E3 ubiquitin-protein ligase CHFR
Intramolecular
Cysteine 635 and cysteine 641
Cysteine 524 and cysteine 529 L
Cysteine 510 and cysteine 513
Cysteine 485 and cysteine 488
Cysteine 510 and cysteine 604
Cysteine 510 and cysteine 601
Cysteine 487 and cysteine 529 L
Cysteine 428 and cysteine 431
Cysteine 431 and cysteine 476
Cysteine 488 and cysteine 524
More...Cysteine 529 and cysteine 532 L
Cysteine 428 and cysteine 476
Cysteine 487 and cysteine 524
Cysteine 513 and cysteine 604
Cysteine 487 and cysteine 532 L
Cysteine 513 and cysteine 601
Cysteine 488 and cysteine 518
Cysteine 601 and cysteine 604
Cysteine 485 and cysteine 524
Cysteine 518 and cysteine 524
Cysteine 524 and cysteine 532 L
Cysteine 485 and cysteine 487
Cysteine 487 and cysteine 488
Cysteine 485 and cysteine 529 L
Cysteine 488 and cysteine 529 L
Cysteine 518 and cysteine 529 L
Cysteine 641 and cysteine 657
Cysteine 485 and cysteine 518
Cysteine 487 and cysteine 518
Cysteine 601 and cysteine 603
Cysteine 488 and cysteine 532 L
Cysteine 635 and cysteine 657
Cysteine 485 and cysteine 532 L
Cysteine 510 and cysteine 603
Cysteine 603 and cysteine 604
Cysteine 513 and cysteine 603
Cysteine 518 and cysteine 532 L
Cysteine 487 and cysteine 603
Cysteine 46 and cysteine 61
Cysteine 487 and cysteine 601
2xoz A 635 A 641
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 635 and 641.
Details
Redox score ?
92
PDB code
2xoz
Structure name
c-terminal cysteine rich domain of human chfr bound to amp
Structure deposition date
2010-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
0
% buried
76
Peptide accession
Q96EP1
Residue number A
635
Residue number B
641
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 635 of E3 ubiquitin-protein ligase CHFR
Cysteine 641 of E3 ubiquitin-protein ligase CHFR
2xoy B 524 B 529
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 524 and 529.
Details
Redox score ?
90
PDB code
2xoy
Structure name
c-terminal cysteine-rich domain of human chfr bound to p(1), p(2)-diadenosine-5'-pyrophosphate
Structure deposition date
2010-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
26
Peptide accession
Q96EP1
Residue number A
524
Residue number B
529
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 524 of E3 ubiquitin-protein ligase CHFR
Cysteine 529 of E3 ubiquitin-protein ligase CHFR
2xoc B 510 B 513
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 510 and 513.
Details
Redox score ?
89
PDB code
2xoc
Structure name
c-terminal cysteine-rich domain of human chfr bound to madpr
Structure deposition date
2010-08-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
3
% buried
33
Peptide accession
Q96EP1
Residue number A
510
Residue number B
513
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 510 of E3 ubiquitin-protein ligase CHFR
Cysteine 513 of E3 ubiquitin-protein ligase CHFR
2xoy B 485 B 488
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 485 and 488.
Details
Redox score ?
89
PDB code
2xoy
Structure name
c-terminal cysteine-rich domain of human chfr bound to p(1), p(2)-diadenosine-5'-pyrophosphate
Structure deposition date
2010-08-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
58
Minimum pKa ?
5
% buried
32
Peptide accession
Q96EP1
Residue number A
485
Residue number B
488
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 485 of E3 ubiquitin-protein ligase CHFR
Cysteine 488 of E3 ubiquitin-protein ligase CHFR
2xoy A 510 A 604
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 510 and 604.
Details
Redox score ?
88
PDB code
2xoy
Structure name
c-terminal cysteine-rich domain of human chfr bound to p(1), p(2)-diadenosine-5'-pyrophosphate
Structure deposition date
2010-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
3
% buried
40
Peptide accession
Q96EP1
Residue number A
510
Residue number B
604
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 510 of E3 ubiquitin-protein ligase CHFR
Cysteine 604 of E3 ubiquitin-protein ligase CHFR
2xp0 A 510 A 601
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 510 and 601.
Details
Redox score ?
85
PDB code
2xp0
Structure name
c-terminal cysteine-rich domain of human chfr
Structure deposition date
2010-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
3
% buried
51
Peptide accession
Q96EP1
Residue number A
510
Residue number B
601
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 510 of E3 ubiquitin-protein ligase CHFR
Cysteine 601 of E3 ubiquitin-protein ligase CHFR
2xp0 B 487 B 529
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 487 and 529.
Details
Redox score ?
85
PDB code
2xp0
Structure name
c-terminal cysteine-rich domain of human chfr
Structure deposition date
2010-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
22
Peptide accession
Q96EP1
Residue number A
487
Residue number B
529
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 487 of E3 ubiquitin-protein ligase CHFR
Cysteine 529 of E3 ubiquitin-protein ligase CHFR
2xoz B 428 B 431
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 428 and 431.
Details
Redox score ?
82
PDB code
2xoz
Structure name
c-terminal cysteine rich domain of human chfr bound to amp
Structure deposition date
2010-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
7
% buried
24
Peptide accession
Q96EP1
Residue number A
428
Residue number B
431
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 428 of E3 ubiquitin-protein ligase CHFR
Cysteine 431 of E3 ubiquitin-protein ligase CHFR
2xoc A 431 A 476
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 431 and 476.
Details
Redox score ?
82
PDB code
2xoc
Structure name
c-terminal cysteine-rich domain of human chfr bound to madpr
Structure deposition date
2010-08-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
7
% buried
18
Peptide accession
Q96EP1
Residue number A
431
Residue number B
476
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 431 of E3 ubiquitin-protein ligase CHFR
Cysteine 476 of E3 ubiquitin-protein ligase CHFR
2xoy B 488 B 524
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 488 and 524.
Details
Redox score ?
82
PDB code
2xoy
Structure name
c-terminal cysteine-rich domain of human chfr bound to p(1), p(2)-diadenosine-5'-pyrophosphate
Structure deposition date
2010-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
24
Peptide accession
Q96EP1
Residue number A
488
Residue number B
524
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 488 of E3 ubiquitin-protein ligase CHFR
Cysteine 524 of E3 ubiquitin-protein ligase CHFR
2xoy A 529 A 532
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 529 and 532.
Details
Redox score ?
81
PDB code
2xoy
Structure name
c-terminal cysteine-rich domain of human chfr bound to p(1), p(2)-diadenosine-5'-pyrophosphate
Structure deposition date
2010-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
6
% buried
38
Peptide accession
Q96EP1
Residue number A
529
Residue number B
532
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 529 of E3 ubiquitin-protein ligase CHFR
Cysteine 532 of E3 ubiquitin-protein ligase CHFR
2xoz A 428 A 476
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 428 and 476.
Details
Redox score ?
81
PDB code
2xoz
Structure name
c-terminal cysteine rich domain of human chfr bound to amp
Structure deposition date
2010-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
31
Peptide accession
Q96EP1
Residue number A
428
Residue number B
476
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 428 of E3 ubiquitin-protein ligase CHFR
Cysteine 476 of E3 ubiquitin-protein ligase CHFR
2xoy B 487 B 524
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 487 and 524.
Details
Redox score ?
81
PDB code
2xoy
Structure name
c-terminal cysteine-rich domain of human chfr bound to p(1), p(2)-diadenosine-5'-pyrophosphate
Structure deposition date
2010-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
8
% buried
24
Peptide accession
Q96EP1
Residue number A
487
Residue number B
524
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 487 of E3 ubiquitin-protein ligase CHFR
Cysteine 524 of E3 ubiquitin-protein ligase CHFR
2xoc A 513 A 604
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 513 and 604.
Details
Redox score ?
75
PDB code
2xoc
Structure name
c-terminal cysteine-rich domain of human chfr bound to madpr
Structure deposition date
2010-08-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
30
Peptide accession
Q96EP1
Residue number A
513
Residue number B
604
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 513 of E3 ubiquitin-protein ligase CHFR
Cysteine 604 of E3 ubiquitin-protein ligase CHFR
2xoc B 487 B 532
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 487 and 532.
Details
Redox score ?
74
PDB code
2xoc
Structure name
c-terminal cysteine-rich domain of human chfr bound to madpr
Structure deposition date
2010-08-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
7
% buried
34
Peptide accession
Q96EP1
Residue number A
487
Residue number B
532
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 487 of E3 ubiquitin-protein ligase CHFR
Cysteine 532 of E3 ubiquitin-protein ligase CHFR
2xoy A 513 A 601
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 513 and 601.
Details
Redox score ?
74
PDB code
2xoy
Structure name
c-terminal cysteine-rich domain of human chfr bound to p(1), p(2)-diadenosine-5'-pyrophosphate
Structure deposition date
2010-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
38
Peptide accession
Q96EP1
Residue number A
513
Residue number B
601
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 513 of E3 ubiquitin-protein ligase CHFR
Cysteine 601 of E3 ubiquitin-protein ligase CHFR
2xoz A 488 A 518
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 488 and 518.
Details
Redox score ?
74
PDB code
2xoz
Structure name
c-terminal cysteine rich domain of human chfr bound to amp
Structure deposition date
2010-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
34
Peptide accession
Q96EP1
Residue number A
488
Residue number B
518
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 488 of E3 ubiquitin-protein ligase CHFR
Cysteine 518 of E3 ubiquitin-protein ligase CHFR
2xoy B 601 B 604
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 601 and 604.
Details
Redox score ?
73
PDB code
2xoy
Structure name
c-terminal cysteine-rich domain of human chfr bound to p(1), p(2)-diadenosine-5'-pyrophosphate
Structure deposition date
2010-08-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
36
Peptide accession
Q96EP1
Residue number A
601
Residue number B
604
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 601 of E3 ubiquitin-protein ligase CHFR
Cysteine 604 of E3 ubiquitin-protein ligase CHFR
2xoz A 485 A 524
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 485 and 524.
Details
Redox score ?
72
PDB code
2xoz
Structure name
c-terminal cysteine rich domain of human chfr bound to amp
Structure deposition date
2010-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
nan
Peptide accession
Q96EP1
Residue number A
485
Residue number B
524
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 485 of E3 ubiquitin-protein ligase CHFR
Cysteine 524 of E3 ubiquitin-protein ligase CHFR
2xoc A 518 A 524
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 518 and 524.
Details
Redox score ?
72
PDB code
2xoc
Structure name
c-terminal cysteine-rich domain of human chfr bound to madpr
Structure deposition date
2010-08-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
36
Peptide accession
Q96EP1
Residue number A
518
Residue number B
524
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 518 of E3 ubiquitin-protein ligase CHFR
Cysteine 524 of E3 ubiquitin-protein ligase CHFR
2xoz A 524 A 532
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 524 and 532.
Details
Redox score ?
71
PDB code
2xoz
Structure name
c-terminal cysteine rich domain of human chfr bound to amp
Structure deposition date
2010-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
38
Peptide accession
Q96EP1
Residue number A
524
Residue number B
532
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 524 of E3 ubiquitin-protein ligase CHFR
Cysteine 532 of E3 ubiquitin-protein ligase CHFR
2xoy A 485 A 487
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 485 and 487.
Details
Redox score ?
71
PDB code
2xoy
Structure name
c-terminal cysteine-rich domain of human chfr bound to p(1), p(2)-diadenosine-5'-pyrophosphate
Structure deposition date
2010-08-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
nan
Peptide accession
Q96EP1
Residue number A
485
Residue number B
487
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 485 of E3 ubiquitin-protein ligase CHFR
Cysteine 487 of E3 ubiquitin-protein ligase CHFR
2xp0 A 487 A 488
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 487 and 488.
Details
Redox score ?
68
PDB code
2xp0
Structure name
c-terminal cysteine-rich domain of human chfr
Structure deposition date
2010-08-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
23
Peptide accession
Q96EP1
Residue number A
487
Residue number B
488
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 487 of E3 ubiquitin-protein ligase CHFR
Cysteine 488 of E3 ubiquitin-protein ligase CHFR
2xoz B 485 B 529
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 485 and 529.
Details
Redox score ?
67
PDB code
2xoz
Structure name
c-terminal cysteine rich domain of human chfr bound to amp
Structure deposition date
2010-08-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
nan
Peptide accession
Q96EP1
Residue number A
485
Residue number B
529
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 485 of E3 ubiquitin-protein ligase CHFR
Cysteine 529 of E3 ubiquitin-protein ligase CHFR
2xoy B 488 B 529
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 488 and 529.
Details
Redox score ?
67
PDB code
2xoy
Structure name
c-terminal cysteine-rich domain of human chfr bound to p(1), p(2)-diadenosine-5'-pyrophosphate
Structure deposition date
2010-08-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
24
Peptide accession
Q96EP1
Residue number A
488
Residue number B
529
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 488 of E3 ubiquitin-protein ligase CHFR
Cysteine 529 of E3 ubiquitin-protein ligase CHFR
2xoy A 518 A 529
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 518 and 529.
Details
Redox score ?
62
PDB code
2xoy
Structure name
c-terminal cysteine-rich domain of human chfr bound to p(1), p(2)-diadenosine-5'-pyrophosphate
Structure deposition date
2010-08-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
6
% buried
35
Peptide accession
Q96EP1
Residue number A
518
Residue number B
529
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 518 of E3 ubiquitin-protein ligase CHFR
Cysteine 529 of E3 ubiquitin-protein ligase CHFR
2xoy A 641 A 657
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 641 and 657.
Details
Redox score ?
62
PDB code
2xoy
Structure name
c-terminal cysteine-rich domain of human chfr bound to p(1), p(2)-diadenosine-5'-pyrophosphate
Structure deposition date
2010-08-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
1
% buried
60
Peptide accession
Q96EP1
Residue number A
641
Residue number B
657
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 641 of E3 ubiquitin-protein ligase CHFR
Cysteine 657 of E3 ubiquitin-protein ligase CHFR
2xp0 B 485 B 518
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 485 and 518.
Details
Redox score ?
62
PDB code
2xp0
Structure name
c-terminal cysteine-rich domain of human chfr
Structure deposition date
2010-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
15
% buried
nan
Peptide accession
Q96EP1
Residue number A
485
Residue number B
518
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 485 of E3 ubiquitin-protein ligase CHFR
Cysteine 518 of E3 ubiquitin-protein ligase CHFR
2xp0 B 487 B 518
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 487 and 518.
Details
Redox score ?
61
PDB code
2xp0
Structure name
c-terminal cysteine-rich domain of human chfr
Structure deposition date
2010-08-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
69
Minimum pKa ?
6
% buried
32
Peptide accession
Q96EP1
Residue number A
487
Residue number B
518
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 487 of E3 ubiquitin-protein ligase CHFR
Cysteine 518 of E3 ubiquitin-protein ligase CHFR
2xoc B 601 B 603
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 601 and 603.
Details
Redox score ?
60
PDB code
2xoc
Structure name
c-terminal cysteine-rich domain of human chfr bound to madpr
Structure deposition date
2010-08-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
71
Minimum pKa ?
9
% buried
36
Peptide accession
Q96EP1
Residue number A
601
Residue number B
603
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 601 of E3 ubiquitin-protein ligase CHFR
Cysteine 603 of E3 ubiquitin-protein ligase CHFR
2xoy A 488 A 532
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 488 and 532.
Details
Redox score ?
60
PDB code
2xoy
Structure name
c-terminal cysteine-rich domain of human chfr bound to p(1), p(2)-diadenosine-5'-pyrophosphate
Structure deposition date
2010-08-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
67
Minimum pKa ?
8
% buried
36
Peptide accession
Q96EP1
Residue number A
488
Residue number B
532
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 488 of E3 ubiquitin-protein ligase CHFR
Cysteine 532 of E3 ubiquitin-protein ligase CHFR
2xoc B 635 B 657
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 635 and 657. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
2xoc
Structure name
c-terminal cysteine-rich domain of human chfr bound to madpr
Structure deposition date
2010-08-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
37
Peptide accession
Q96EP1
Residue number A
635
Residue number B
657
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 635 of E3 ubiquitin-protein ligase CHFR
Cysteine 657 of E3 ubiquitin-protein ligase CHFR
2xp0 B 485 B 532
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 485 and 532. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
2xp0
Structure name
c-terminal cysteine-rich domain of human chfr
Structure deposition date
2010-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
16
% buried
nan
Peptide accession
Q96EP1
Residue number A
485
Residue number B
532
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 485 of E3 ubiquitin-protein ligase CHFR
Cysteine 532 of E3 ubiquitin-protein ligase CHFR
2xp0 B 510 B 603
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 510 and 603. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
2xp0
Structure name
c-terminal cysteine-rich domain of human chfr
Structure deposition date
2010-08-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
3
% buried
32
Peptide accession
Q96EP1
Residue number A
510
Residue number B
603
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 510 of E3 ubiquitin-protein ligase CHFR
Cysteine 603 of E3 ubiquitin-protein ligase CHFR
2xp0 A 603 A 604
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 603 and 604. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
2xp0
Structure name
c-terminal cysteine-rich domain of human chfr
Structure deposition date
2010-08-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
34
Peptide accession
Q96EP1
Residue number A
603
Residue number B
604
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 603 of E3 ubiquitin-protein ligase CHFR
Cysteine 604 of E3 ubiquitin-protein ligase CHFR
2xoc B 513 B 603
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 513 and 603. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
2xoc
Structure name
c-terminal cysteine-rich domain of human chfr bound to madpr
Structure deposition date
2010-08-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
22
Peptide accession
Q96EP1
Residue number A
513
Residue number B
603
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 513 of E3 ubiquitin-protein ligase CHFR
Cysteine 603 of E3 ubiquitin-protein ligase CHFR
2xp0 B 518 B 532
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 518 and 532. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
2xp0
Structure name
c-terminal cysteine-rich domain of human chfr
Structure deposition date
2010-08-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
82
Minimum pKa ?
15
% buried
46
Peptide accession
Q96EP1
Residue number A
518
Residue number B
532
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 518 of E3 ubiquitin-protein ligase CHFR
Cysteine 532 of E3 ubiquitin-protein ligase CHFR
2xoz A 487 A 603
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 487 and 603. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
2xoz
Structure name
c-terminal cysteine rich domain of human chfr bound to amp
Structure deposition date
2010-08-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
6
% buried
28
Peptide accession
Q96EP1
Residue number A
487
Residue number B
603
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 487 of E3 ubiquitin-protein ligase CHFR
Cysteine 603 of E3 ubiquitin-protein ligase CHFR
1lgq A 46 A 61
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 46 and 61. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
1lgq
Structure name
crystal structure of the fha domain of the chfr mitotic checkpoint protein
Structure deposition date
2002-04-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
58
Peptide accession
Q96EP1
Residue number A
46
Residue number B
61
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 46 of E3 ubiquitin-protein ligase CHFR
Cysteine 61 of E3 ubiquitin-protein ligase CHFR
2xoc A 487 A 601
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHFR between cysteines 487 and 601. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2xoc
Structure name
c-terminal cysteine-rich domain of human chfr bound to madpr
Structure deposition date
2010-08-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
8
% buried
39
Peptide accession
Q96EP1
Residue number A
487
Residue number B
601
Peptide name
E3 ubiquitin-protein ligase CHFR
Ligandability
Cysteine 487 of E3 ubiquitin-protein ligase CHFR
Cysteine 601 of E3 ubiquitin-protein ligase CHFR
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